γ-Glutamyl transferase (γ-GTP) was purified from renal cortex tissue by means of Miller's method to study on the heterogenity of this enzyme in hepatocellular carcinoma (HCC). Finally, two forms of γ-GTP, in which one had a capacity to bind to Con A and another did not bind to this lecitin, were separated through Con A sepharose column chromatography. Purified Con A bound γ -GTP showed 3 protein bands on the polyacrylamide gel electrophoresis, which were also positive for γ -GTP stain, while another form was identified with a single protein band. By using antiserum against Con A unbound γ -GTP, γ -GTP was localized in 40% cases of 30 tissue specimens of HCC. In conclusion, the purified γ -GTP could be a useful marker protein for analyzing the origin of HCC specific γ -GTP in the patient sera with HCC.